Detection of Ca2+-dependent transglutaminase activity in root and leaf tissue of monocotyledonous and dicotyledonous plants

Graham R. Lilley, James Skill, Martin Griffin, Philip L.R. Bonner

Research output: Contribution to journalArticlepeer-review

69 Scopus citations

Abstract

Protein extracted from root and leaf tissue of the dicotyledonous plants pea (Pisum sativum) and broad bean (Vicia faba) and the monocotyledonous plants wheat (Triticum aestivum) and barley (Hordeum vulgare) were shown to catalyze the incorporation of biotin-labeled cadaverine into microtiter-plate-bound N′,N′-dimethylcasein and the cross-linking of biotin-labeled casein to microtiter-plate-bound casein in a Ca2+-dependent manner. The cross-linking of biotinylated casein and the incorporation of biotinlabeled cadaverine into N′,N′-dimethylcasein were time-dependent reactions with a pH optimum of 7.9. Transglutaminase activity was shown to increase over a 2-week growth period in both the roots and leaves of pea. The product of transglutaminase's protein-crosslinking activity, ∈-(γ-glutamyl)-lysine isodipeptide, was detected in root and shoot protein from pea, broad bean, wheat, and barley by cation-exchange chromatography. The presence of the isodipeptide was confirmed by reversed-phase chromatography. Hydrolysis of the isodipeptide after cation-exchange chromatography confirmed the presence of glutamate and lysine.

Original languageEnglish (US)
Pages (from-to)1115-1123
Number of pages9
JournalPlant Physiology
Volume117
Issue number3
DOIs
StatePublished - 1998

ASJC Scopus subject areas

  • Physiology
  • Genetics
  • Plant Science

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